Interleukin enhancer-binding factor 3 (ILF3)

Interleukin enhancer-binding factor 3 (ILF3) is a ubiquitously expressed, multifunctional RNA-binding protein that forms heterodimers (notably with ILF2/NF45) and regulates various aspects of gene expression, particularly at the mRNA level[1][2][4]. It binds to double-stranded and structured RNAs, facilitating mRNA stabilization, influencing splicing, promoting circular RNA (circRNA) biogenesis, and participating in microRNA processing[2][4]. ILF3 is crucial for T-cell activation (regulating interleukin-2 expression), response to cellular stress, and orchestration of innate antiviral defense (influencing HIV, hepatitis B, dengue, and other RNA viruses)[2][1][4]. It is implicated as an autoantigen in autoimmunity, shows altered expression in several cancers and proliferative disorders, and is a hub for post-transcriptional regulatory networks fundamental to normal and pathological cell function[1][2][4]. ILF3 contains two double-stranded RNA binding motifs and an N-terminal DZF domain, allowing wide interaction with RNAs and protein complexes[5]. Targeting ILF3 pharmacologically remains investigational due to its centrality in RNA metabolism and potential for broad systemic effects.

Other names

MPHOSPH4DRBP76NF90MPP4Nuclear factor of activated T-cells 90 kDaTranslational control protein 80M-phase phosphoprotein 4NFAR110NF110NF90ctvMPP4110NFAR-1NFAR-2TCP110NFAR90NF110bNF90aNF90cDouble-stranded RNA-binding protein 76Nuclear factor associated with dsRNADsRNA binding protein NFAR-2/MPP4NF-AT-90TCP80DRBFNFARCBTFMMP4NF90bNFAR2Nuclear factor associated with DS RNA

Not applicable/unknown for clinical drugs; theoretical actions would include inhibition of RNA-binding, modulation of phosphorylation to inhibit post-transcriptional regulatory functions, or interference with heterodimerization with ILF2. Expression and phosphorylation state may be influenced indirectly by drugs modulating PKR or other pathways.